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IPR008880 is a Trigger factor, C-terminal.
<p>In the Escherichia coli cytosol, a fraction of the newly synthesised proteins requires the activity of molecular chaperones for folding to the native state. The major chaperones implicated in this folding process are the ribosome-associated Trigger Factor (TF), and the DnaK and GroEL chaperones with their respective co-chaperones. Trigger Factor is an ATP-independent chaperone and displays chaperone and peptidyl-prolyl-cis-trans-isomerase (PPIase) activities<i>in vitro</i>. It is composed of three domains, an N-terminal ribosome-binding domain (RBD) which mediates association with the large ribosomal subunit, a central PPIase domain with homology to FKBP proteins, and a C-terminal substrate-binding domain (SBD) which forms the central body of the protein and has two helical arms that create a cavity [[cite:PUB00099906]]. The association between its N-terminal domain with the ribosomal protein L23 located next to the peptide tunnel exit is essential for the interaction with nascent polypeptides and its in vivo function [[cite:PUB00011507]].</p> <p>This entry represents the C-terminal domain of bacterial TF proteins, which has a multi-helical structure consisting of an irregular array of long and short helices. This domain is structurally similar to the peptide-binding domain of the bacterial porin chaperone SurA [[cite:PUB00099907]].</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Biological process | Protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. | ||
| Biological process | Protein transport | The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: trigger factor-like [Glycine max] gi|356552817|ref|XP_003544759.1| | 7 | ||
| – | Trigger factor; TAIR: AT5G55220.1 trigger factor type chaperone family protein; Swiss-Prot: sp|Q8S9L5|TIG_ARATH Trigger factor-like protein TIG, Chloroplastic; TrEMBL-Plants: tr|I1JJE0|I1JJE0_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0024000 | 23 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| SSF54534 | SUPERFAMILY | 1 | 50.00 |